TPDB

3D PDB MODEL

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TPDB ID TPDB46928

Peptide_Name

ACE inhibitor

Activity

ACE inhibitors Antihypertensive Bitter

Activity_category_statistics

Cardiometabolic peptides Food sensory peptides

Database_Source

Peptipedia AHTPDB AHTpin Tastepeptides-Meta

Sequence_Type

standard

Has_Modification No

Description A 9-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, and Bitter) peptide sequence curated from Peptipedia, AHTPDB, AHTpin, and other sources, with an available 3D structural model.

Sequence

IVGRPRHQG

FASTA

>TPDB46928|ACE inhibitors;Antihypertensive;Bitter|length=9
IVGRPRHQG

Formula C43H74N18O11

Absent Amino Acids ANDCELKMFSTWY

Common Amino Acids RG

Mass 1019.17

PI 12.40

Basic Residues 3

Acidic Residues 0

Hydrophobic Residues 2

Net Charge +2

Boman Index 3.39

Hydrophobicity -1.044

Aliphatic Index 75.56

Half Life

Mammalian: 20 hour Yeast: 30 min E.coli: >10 hour

Extinction Coefficient Cystines 0

Absorbance 280nm 0.00

Polar Residues 1

number

0

A

2

R

0

N

0

D

0

C

0

E

1

Q

2

G

1

H

1

I

0

L

0

K

0

M

0

F

1

P

0

S

0

T

0

W

0

Y

1

V

Amino Acid Distribution

A: 0 R: 2 N: 0 D: 0 C: 0 E: 0 Q: 1 G: 2 H: 1 I: 1 L: 0 K: 0 M: 0 F: 0 P: 1 S: 0 T: 0 W: 0 Y: 0 V: 1

Length

9

Formula

C43H74N18O11

Mass

1019.17

PI

12.40

Net Charge

+2

Boman Index

3.39

Hydrophobicity

-1.044

Chemical_Mass

1019.1587

Monoisotopic_Mass

1018.5769

Evidence 1 Activity

Activity

Activity Endpoint IC50

Detail Source Activity ACE inhibitors

Activity Measurement 2.40 µM

Function Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: XM02-001)

Detail Activity ACE inhibitor

Activity Code ah

Source & Reference

Database Source NA

Authors Yokoyama K., Chiba H., and Yoshikawa M.

Title

Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci. Biotech. Biochem., 56, 1541-1545

Year 1992

Literature Source Journal

Other

Number of Residues 9

Additional Info

BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)([C@@H](C)CC)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)N1CCC[C@@]1([H])C(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)N[C@@]([H])(CC1=CN=CN1)C(=O)N[C@@]([H])(CCC(N)=O)C(=O)NCC(O)=O InChI=1S/C43H74N18O11/c1-5-23(4)33(45)39(70)60-34(22(2)3)40(71)53-19-31(63)56-27(10-7-15-52-43(48)49)41(72)61-16-8-11-29(61)38(69)58-25(9-6-14-51-42(46)47)36(67)59-28(17-24-18-50-21-55-24)37(68)57-26(12-13-30(44)62)35(66)54-20-32(64)65/h18,21-23,25-29,33-34H,5-17,19-20,45H2,1-4H3,(H2,44,62)(H,50,55)(H,53,71)(H,54,66)(H,56,63)(H,57,68)(H,58,69)(H,59,67)(H,60,70)(H,64,65)(H4,46,47,51)(H4,48,49,52)/t23-,25-,26-,27-,28-,29-,33-,34-/m0/s1 InChIKey=FANJYQMTXWNAOX-ZKZGVUGUSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Peptide released from myosin by simulated gastric juice. Terashima M., Baba T., Ikemoto N., Katayama M., Morimoto T., Matsumura S., 2010, Novel angiotensin-converting enzyme (ACE) inhibitory peptides derived from boneless chicken leg meat. J. Agric. Food Chem., 58, 7432-7436

Evidence 2 Activity

Activity

Activity Endpoint IC50

Detail Source Activity Antihypertensive

Activity Measurement 2.40 µM

Function Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: XM02-001)

Detail Activity ACE inhibitor

Activity Code ah

Source & Reference

Database Source AHTPDB

Authors Yokoyama K., Chiba H., and Yoshikawa M.

Title

Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci. Biotech. Biochem., 56, 1541-1545

Year 1992

Literature Source Journal

Other

Source Activity Label	Source Definition
Antihypertensive	AHTPDB manually curated experimentally validated antihypertensive peptide annotation.

Number of Residues 9

Additional Info

BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)([C@@H](C)CC)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)N1CCC[C@@]1([H])C(=O)N[C@@]([H])(CCCNC(N)=N)C(=O)N[C@@]([H])(CC1=CN=CN1)C(=O)N[C@@]([H])(CCC(N)=O)C(=O)NCC(O)=O InChI=1S/C43H74N18O11/c1-5-23(4)33(45)39(70)60-34(22(2)3)40(71)53-19-31(63)56-27(10-7-15-52-43(48)49)41(72)61-16-8-11-29(61)38(69)58-25(9-6-14-51-42(46)47)36(67)59-28(17-24-18-50-21-55-24)37(68)57-26(12-13-30(44)62)35(66)54-20-32(64)65/h18,21-23,25-29,33-34H,5-17,19-20,45H2,1-4H3,(H2,44,62)(H,50,55)(H,53,71)(H,54,66)(H,56,63)(H,57,68)(H,58,69)(H,59,67)(H,60,70)(H,64,65)(H4,46,47,51)(H4,48,49,52)/t23-,25-,26-,27-,28-,29-,33-,34-/m0/s1 InChIKey=FANJYQMTXWNAOX-ZKZGVUGUSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Peptide released from myosin by simulated gastric juice. Terashima M., Baba T., Ikemoto N., Katayama M., Morimoto T., Matsumura S., 2010, Novel angiotensin-converting enzyme (ACE) inhibitory peptides derived from boneless chicken leg meat. J. Agric. Food Chem., 58, 7432-7436

Number_of_Residues

9